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Volumn 22, Issue S2, 2013, Pages

Extracellular matrix components in breast cancer progression and metastasis

Author keywords

Extracellular matrix; Mammary gland involution; Metastatic breast cancer; Metastatic niche; Therapy resistance; Tissue remodeling

Indexed keywords

CATHEPSIN; CATHEPSIN K INHIBITOR; DOXORUBICIN; GELATINASE A; GELATINASE B; HYALURONIC ACID; HYMECROMONE; INTERLEUKIN 2; KALININ; LAMININ; LAMININ 10; LAMININ 111; MATRIX METALLOPROTEINASE 14; OSTEONECTIN; OSTEOPONTIN; PACLITAXEL; PROTEIN LYSINE 6 OXIDASE; STROMELYSIN; TENASCIN; THROMBOSPONDIN; TRANSCRIPTION FACTOR RUNX2; UNCLASSIFIED DRUG; UROKINASE;

EID: 84884709908     PISSN: 09609776     EISSN: 15323080     Source Type: Journal    
DOI: 10.1016/j.breast.2013.07.012     Document Type: Article
Times cited : (233)

References (104)
  • 1
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: not just pretty fibrils
    • Hynes R.O. The extracellular matrix: not just pretty fibrils. Science 2009, 326:1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 5
    • 0036153330 scopus 로고    scopus 로고
    • Normal and tumor-derived myoepithelial cells differ in their ability to interact with luminal breast epithelial cells for polarity and basement membrane deposition
    • Gudjonsson T., Ronnov-Jessen L., Villadsen R., Rank F., Bissell M.J., Petersen O.W. Normal and tumor-derived myoepithelial cells differ in their ability to interact with luminal breast epithelial cells for polarity and basement membrane deposition. Journal of Cell Science 2002, 115:39-50.
    • (2002) Journal of Cell Science , vol.115 , pp. 39-50
    • Gudjonsson, T.1    Ronnov-Jessen, L.2    Villadsen, R.3    Rank, F.4    Bissell, M.J.5    Petersen, O.W.6
  • 6
    • 67649336911 scopus 로고    scopus 로고
    • Extracellular matrix controls insulin signaling in mammary epithelial cells through the RhoA/Rok pathway
    • Lee Y.J., Hsu T.C., Du J.Y., et al. Extracellular matrix controls insulin signaling in mammary epithelial cells through the RhoA/Rok pathway. Journal of Cellular Physiology 2009, 220:476-484.
    • (2009) Journal of Cellular Physiology , vol.220 , pp. 476-484
    • Lee, Y.J.1    Hsu, T.C.2    Du, J.Y.3
  • 8
    • 0028940340 scopus 로고
    • Laminin mediates tissue-specific gene expression in mammary epithelia
    • Streuli C.H., Schmidhauser C., Bailey N., et al. Laminin mediates tissue-specific gene expression in mammary epithelia. Journal of Cell Biology 1995, 129:591-603.
    • (1995) Journal of Cell Biology , vol.129 , pp. 591-603
    • Streuli, C.H.1    Schmidhauser, C.2    Bailey, N.3
  • 10
    • 27944467950 scopus 로고    scopus 로고
    • Ablation of beta1 integrin in mammary epithelium reveals a key role for integrin in glandular morphogenesis and differentiation
    • Naylor M.J., Li N., Cheung J., et al. Ablation of beta1 integrin in mammary epithelium reveals a key role for integrin in glandular morphogenesis and differentiation. Journal of Cell Biology 2005, 171:717-728.
    • (2005) Journal of Cell Biology , vol.171 , pp. 717-728
    • Naylor, M.J.1    Li, N.2    Cheung, J.3
  • 12
    • 84867444588 scopus 로고    scopus 로고
    • Rat mammary extracellular matrix composition and response to ibuprofen treatment during postpartum involution by differential GeLC-MS/MS analysis
    • O'Brien J.H., Vanderlinden L.A., Schedin P.J., Hansen K.C. Rat mammary extracellular matrix composition and response to ibuprofen treatment during postpartum involution by differential GeLC-MS/MS analysis. Journal of Proteome Research 2012, 11:4894-4905.
    • (2012) Journal of Proteome Research , vol.11 , pp. 4894-4905
    • O'Brien, J.H.1    Vanderlinden, L.A.2    Schedin, P.J.3    Hansen, K.C.4
  • 13
    • 80052499480 scopus 로고    scopus 로고
    • Postpartum mammary gland involution drives progression of ductal carcinoma in situ through collagen and COX-2
    • Lyons T.R., O'Brien J., Borges V.F., et al. Postpartum mammary gland involution drives progression of ductal carcinoma in situ through collagen and COX-2. Nature Medicine 2011, 17:1109-1115.
    • (2011) Nature Medicine , vol.17 , pp. 1109-1115
    • Lyons, T.R.1    O'Brien, J.2    Borges, V.F.3
  • 14
    • 0034234253 scopus 로고    scopus 로고
    • Reproductive state of rat mammary gland stroma modulates human breast cancer cell migration and invasion
    • Bemis L.T., Schedin P. Reproductive state of rat mammary gland stroma modulates human breast cancer cell migration and invasion. Cancer Research 2000, 60:3414-3418.
    • (2000) Cancer Research , vol.60 , pp. 3414-3418
    • Bemis, L.T.1    Schedin, P.2
  • 15
    • 33144465789 scopus 로고    scopus 로고
    • Remodeling of the mammary microenvironment after lactation promotes breast tumor cell metastasis
    • McDaniel S.M., Rumer K.K., Biroc S.L., et al. Remodeling of the mammary microenvironment after lactation promotes breast tumor cell metastasis. American Journal of Pathology 2006, 168:608-620.
    • (2006) American Journal of Pathology , vol.168 , pp. 608-620
    • McDaniel, S.M.1    Rumer, K.K.2    Biroc, S.L.3
  • 16
    • 33645322443 scopus 로고    scopus 로고
    • Pregnancy-associated breast cancer and metastasis
    • Schedin P. Pregnancy-associated breast cancer and metastasis. Nature Reviews Cancer 2006, 6:281-291.
    • (2006) Nature Reviews Cancer , vol.6 , pp. 281-291
    • Schedin, P.1
  • 17
    • 77749264278 scopus 로고    scopus 로고
    • Alternatively activated macrophages and collagen remodeling characterize the postpartum involuting mammary gland across species
    • O'Brien J., Lyons T., Monks J., et al. Alternatively activated macrophages and collagen remodeling characterize the postpartum involuting mammary gland across species. American Journal of Pathology 2010, 176:1241-1255.
    • (2010) American Journal of Pathology , vol.176 , pp. 1241-1255
    • O'Brien, J.1    Lyons, T.2    Monks, J.3
  • 18
    • 63049104211 scopus 로고    scopus 로고
    • Microenvironmental regulation of metastasis
    • Joyce J.A., Pollard J.W. Microenvironmental regulation of metastasis. Nature Reviews Cancer 2009, 9:239-252.
    • (2009) Nature Reviews Cancer , vol.9 , pp. 239-252
    • Joyce, J.A.1    Pollard, J.W.2
  • 19
    • 0029312252 scopus 로고
    • Involvement of extracellular matrix constituents in breast cancer
    • Lochter A., Bissell M.J. Involvement of extracellular matrix constituents in breast cancer. Seminars in Cancer Biology 1995, 6:165-173.
    • (1995) Seminars in Cancer Biology , vol.6 , pp. 165-173
    • Lochter, A.1    Bissell, M.J.2
  • 20
    • 0034609730 scopus 로고    scopus 로고
    • Restoration of positioning control following disabled-2 expression in ovarian and breast tumor cells
    • Sheng Z., Sun W., Smith E., Cohen C., Xu X.X. Restoration of positioning control following disabled-2 expression in ovarian and breast tumor cells. Oncogene 2000, 19:4847-4854.
    • (2000) Oncogene , vol.19 , pp. 4847-4854
    • Sheng, Z.1    Sun, W.2    Smith, E.3    Cohen, C.4    Xu, X.X.5
  • 21
    • 0037437146 scopus 로고    scopus 로고
    • Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution
    • Schenk S., Hintermann E., Bilban M., et al. Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution. Journal of Cell Biology 2003, 161:197-209.
    • (2003) Journal of Cell Biology , vol.161 , pp. 197-209
    • Schenk, S.1    Hintermann, E.2    Bilban, M.3
  • 22
    • 84861819901 scopus 로고    scopus 로고
    • Invasive breast cancer induces laminin-332 upregulation and integrin beta4 neoexpression in myofibroblasts to confer an anoikis-resistant phenotype during tissue remodeling
    • Kim B.G., Gao M.Q., Choi Y.P., et al. Invasive breast cancer induces laminin-332 upregulation and integrin beta4 neoexpression in myofibroblasts to confer an anoikis-resistant phenotype during tissue remodeling. Breast Cancer Research: BCR 2012, 14:R88.
    • (2012) Breast Cancer Research: BCR , vol.14
    • Kim, B.G.1    Gao, M.Q.2    Choi, Y.P.3
  • 24
    • 65549119715 scopus 로고    scopus 로고
    • Motility induction in breast carcinoma by mammary epithelial laminin 332 (laminin 5)
    • Carpenter P.M., Dao A.V., Arain Z.S., et al. Motility induction in breast carcinoma by mammary epithelial laminin 332 (laminin 5). Molecular Cancer Research: MCR 2009, 7:462-475.
    • (2009) Molecular Cancer Research: MCR , vol.7 , pp. 462-475
    • Carpenter, P.M.1    Dao, A.V.2    Arain, Z.S.3
  • 25
    • 84872200089 scopus 로고    scopus 로고
    • Laminin-511: a multi-functional adhesion protein regulating cell migration, tumor invasion and metastasis
    • Pouliot N., Kusuma N. Laminin-511: a multi-functional adhesion protein regulating cell migration, tumor invasion and metastasis. Cell Adhesion & Migration 2013, 7:142-149.
    • (2013) Cell Adhesion & Migration , vol.7 , pp. 142-149
    • Pouliot, N.1    Kusuma, N.2
  • 28
    • 84870255943 scopus 로고    scopus 로고
    • Increased hyaluronan content and stromal cell CD44 associate with HER2 positivity and poor prognosis in human breast cancer
    • Auvinen P., Tammi R., Kosma V.M., et al. Increased hyaluronan content and stromal cell CD44 associate with HER2 positivity and poor prognosis in human breast cancer. International Journal of Cancer. Journal International du Cancer 2013, 132:531-539.
    • (2013) International Journal of Cancer. Journal International du Cancer , vol.132 , pp. 531-539
    • Auvinen, P.1    Tammi, R.2    Kosma, V.M.3
  • 29
    • 84862909092 scopus 로고    scopus 로고
    • Hyaluronan synthase HAS2 promotes tumor progression in bone by stimulating the interaction of breast cancer stem-like cells with macrophages and stromal cells
    • Okuda H., Kobayashi A., Xia B., et al. Hyaluronan synthase HAS2 promotes tumor progression in bone by stimulating the interaction of breast cancer stem-like cells with macrophages and stromal cells. Cancer Research 2012, 72:537-547.
    • (2012) Cancer Research , vol.72 , pp. 537-547
    • Okuda, H.1    Kobayashi, A.2    Xia, B.3
  • 31
    • 22244442728 scopus 로고    scopus 로고
    • Antisense-mediated suppression of hyaluronan synthase 2 inhibits the tumorigenesis and progression of breast cancer
    • Udabage L., Brownlee G.R., Waltham M., et al. Antisense-mediated suppression of hyaluronan synthase 2 inhibits the tumorigenesis and progression of breast cancer. Cancer Research 2005, 65:6139-6150.
    • (2005) Cancer Research , vol.65 , pp. 6139-6150
    • Udabage, L.1    Brownlee, G.R.2    Waltham, M.3
  • 32
    • 34447530390 scopus 로고    scopus 로고
    • The hyaluronan receptors CD44 and Rhamm (CD168) form complexes with ERK1,2 that sustain high basal motility in breast cancer cells
    • Hamilton S.R., Fard S.F., Paiwand F.F., et al. The hyaluronan receptors CD44 and Rhamm (CD168) form complexes with ERK1,2 that sustain high basal motility in breast cancer cells. Journal of Biological Chemistry 2007, 282:16667-16680.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 16667-16680
    • Hamilton, S.R.1    Fard, S.F.2    Paiwand, F.F.3
  • 33
    • 84856229021 scopus 로고    scopus 로고
    • MT1-MMP protects breast carcinoma cells against type I collagen-induced apoptosis
    • Maquoi E., Assent D., Detilleux J., Pequeux C., Foidart J.M., Noel A. MT1-MMP protects breast carcinoma cells against type I collagen-induced apoptosis. Oncogene 2012, 31:480-493.
    • (2012) Oncogene , vol.31 , pp. 480-493
    • Maquoi, E.1    Assent, D.2    Detilleux, J.3    Pequeux, C.4    Foidart, J.M.5    Noel, A.6
  • 34
    • 0033597726 scopus 로고    scopus 로고
    • The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis
    • Sternlicht M.D., Lochter A., Sympson C.J., et al. The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis. Cell 1999, 98:137-146.
    • (1999) Cell , vol.98 , pp. 137-146
    • Sternlicht, M.D.1    Lochter, A.2    Sympson, C.J.3
  • 35
    • 0035110730 scopus 로고    scopus 로고
    • Overexpression of membrane-type matrix metalloproteinase-1 gene induces mammary gland abnormalities and adenocarcinoma in transgenic mice
    • Ha H.Y., Moon H.B., Nam M.S., et al. Overexpression of membrane-type matrix metalloproteinase-1 gene induces mammary gland abnormalities and adenocarcinoma in transgenic mice. Cancer Research 2001, 61:984-990.
    • (2001) Cancer Research , vol.61 , pp. 984-990
    • Ha, H.Y.1    Moon, H.B.2    Nam, M.S.3
  • 36
    • 0037116616 scopus 로고    scopus 로고
    • Pooled analysis of prognostic impact of urokinase-type plasminogen activator and its inhibitor PAI-1 in 8377 breast cancer patients
    • Look M.P., van Putten W.L., Duffy M.J., et al. Pooled analysis of prognostic impact of urokinase-type plasminogen activator and its inhibitor PAI-1 in 8377 breast cancer patients. Journal of the National Cancer Institute 2002, 94:116-128.
    • (2002) Journal of the National Cancer Institute , vol.94 , pp. 116-128
    • Look, M.P.1    van Putten, W.L.2    Duffy, M.J.3
  • 37
    • 84863229642 scopus 로고    scopus 로고
    • Cathepsin B inhibition limits bone metastasis in breast cancer
    • Withana N.P., Blum G., Sameni M., et al. Cathepsin B inhibition limits bone metastasis in breast cancer. Cancer Research 2012, 72:1199-1209.
    • (2012) Cancer Research , vol.72 , pp. 1199-1209
    • Withana, N.P.1    Blum, G.2    Sameni, M.3
  • 38
    • 81155127516 scopus 로고    scopus 로고
    • Inhibition of cathepsin B activity attenuates extracellular matrix degradation and inflammatory breast cancer invasion
    • Victor B.C., Anbalagan A., Mohamed M.M., Sloane B.F., Cavallo-Medved D. Inhibition of cathepsin B activity attenuates extracellular matrix degradation and inflammatory breast cancer invasion. Breast Cancer Research: BCR 2011, 13:R115.
    • (2011) Breast Cancer Research: BCR , vol.13
    • Victor, B.C.1    Anbalagan, A.2    Mohamed, M.M.3    Sloane, B.F.4    Cavallo-Medved, D.5
  • 39
    • 33744917827 scopus 로고    scopus 로고
    • Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer
    • Vasiljeva O., Papazoglou A., Kruger A., et al. Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer. Cancer Research 2006, 66:5242-5250.
    • (2006) Cancer Research , vol.66 , pp. 5242-5250
    • Vasiljeva, O.1    Papazoglou, A.2    Kruger, A.3
  • 40
    • 35448959223 scopus 로고    scopus 로고
    • Acathepsin K inhibitor reduces breast cancer induced osteolysis and skeletal tumor burden
    • Le Gall C., Bellahcene A., Bonnelye E., et al. Acathepsin K inhibitor reduces breast cancer induced osteolysis and skeletal tumor burden. Cancer Research 2007, 67:9894-9902.
    • (2007) Cancer Research , vol.67 , pp. 9894-9902
    • Le Gall, C.1    Bellahcene, A.2    Bonnelye, E.3
  • 41
    • 33646365644 scopus 로고    scopus 로고
    • Lysyl oxidase is essential for hypoxia-induced metastasis
    • Erler J.T., Bennewith K.L., Nicolau M., et al. Lysyl oxidase is essential for hypoxia-induced metastasis. Nature 2006, 440:1222-1226.
    • (2006) Nature , vol.440 , pp. 1222-1226
    • Erler, J.T.1    Bennewith, K.L.2    Nicolau, M.3
  • 42
    • 70450222098 scopus 로고    scopus 로고
    • Matrix crosslinking forces tumor progression by enhancing integrin signaling
    • Levental K.R., Yu H., Kass L., et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell 2009, 139:891-906.
    • (2009) Cell , vol.139 , pp. 891-906
    • Levental, K.R.1    Yu, H.2    Kass, L.3
  • 43
    • 33749452709 scopus 로고    scopus 로고
    • Tenascin-C induced signaling in cancer
    • Orend G., Chiquet-Ehrismann R. Tenascin-C induced signaling in cancer. Cancer Letters 2006, 244:143-163.
    • (2006) Cancer Letters , vol.244 , pp. 143-163
    • Orend, G.1    Chiquet-Ehrismann, R.2
  • 44
    • 0038582634 scopus 로고    scopus 로고
    • Involvement of large tenascin-C splice variants in breast cancer progression
    • Tsunoda T., Inada H., Kalembeyi I., et al. Involvement of large tenascin-C splice variants in breast cancer progression. American Journal of Pathology 2003, 162:1857-1867.
    • (2003) American Journal of Pathology , vol.162 , pp. 1857-1867
    • Tsunoda, T.1    Inada, H.2    Kalembeyi, I.3
  • 45
    • 79960117895 scopus 로고    scopus 로고
    • Breast cancer cells produce tenascin C as a metastatic niche component to colonize the lungs
    • Oskarsson T., Acharyya S., Zhang X.H., et al. Breast cancer cells produce tenascin C as a metastatic niche component to colonize the lungs. Nature Medicine 2011, 17:867-874.
    • (2011) Nature Medicine , vol.17 , pp. 867-874
    • Oskarsson, T.1    Acharyya, S.2    Zhang, X.H.3
  • 46
    • 38049115129 scopus 로고    scopus 로고
    • Endogenous human microRNAs that suppress breast cancer metastasis
    • Tavazoie S.F., Alarcon C., Oskarsson T., et al. Endogenous human microRNAs that suppress breast cancer metastasis. Nature 2008, 451:147-152.
    • (2008) Nature , vol.451 , pp. 147-152
    • Tavazoie, S.F.1    Alarcon, C.2    Oskarsson, T.3
  • 47
    • 10644246851 scopus 로고    scopus 로고
    • Co-stimulation of human breast cancer cells with transforming growth factor-beta and tenascin-C enhances matrix metalloproteinase-9 expression and cancer cell invasion
    • Ilunga K., Nishiura R., Inada H., et al. Co-stimulation of human breast cancer cells with transforming growth factor-beta and tenascin-C enhances matrix metalloproteinase-9 expression and cancer cell invasion. International Journal of Experimental Pathology 2004, 85:373-379.
    • (2004) International Journal of Experimental Pathology , vol.85 , pp. 373-379
    • Ilunga, K.1    Nishiura, R.2    Inada, H.3
  • 48
    • 68349100337 scopus 로고    scopus 로고
    • Tumour-associated tenascin-C isoforms promote breast cancer cell invasion and growth by matrix metalloproteinase-dependent and independent mechanisms
    • Hancox R.A., Allen M.D., Holliday D.L., et al. Tumour-associated tenascin-C isoforms promote breast cancer cell invasion and growth by matrix metalloproteinase-dependent and independent mechanisms. Breast Cancer Research: BCR 2009, 11:R24.
    • (2009) Breast Cancer Research: BCR , vol.11
    • Hancox, R.A.1    Allen, M.D.2    Holliday, D.L.3
  • 49
    • 0031770515 scopus 로고    scopus 로고
    • Tenascin-C expression in invasion border of early breast cancer: a predictor of local and distant recurrence
    • Jahkola T., Toivonen T., Virtanen I., et al. Tenascin-C expression in invasion border of early breast cancer: a predictor of local and distant recurrence. British Journal of Cancer 1998, 78:1507-1513.
    • (1998) British Journal of Cancer , vol.78 , pp. 1507-1513
    • Jahkola, T.1    Toivonen, T.2    Virtanen, I.3
  • 50
    • 0028905862 scopus 로고
    • Tenascin in breast cancer development - is epithelial tenascin a marker for poor prognosis?
    • Yoshida T., Ishihara A., Hirokawa Y., Kusakabe M., Sakakura T. Tenascin in breast cancer development - is epithelial tenascin a marker for poor prognosis?. Cancer Letters 1995, 90:65-73.
    • (1995) Cancer Letters , vol.90 , pp. 65-73
    • Yoshida, T.1    Ishihara, A.2    Hirokawa, Y.3    Kusakabe, M.4    Sakakura, T.5
  • 53
    • 0034540852 scopus 로고    scopus 로고
    • Adherence to osteopontin via alphavbeta3 suppresses phorbol ester-mediated apoptosis in MCF-7 breast cancer cells that overexpress protein kinase C-alpha
    • Noti J.D. Adherence to osteopontin via alphavbeta3 suppresses phorbol ester-mediated apoptosis in MCF-7 breast cancer cells that overexpress protein kinase C-alpha. International Journal of Oncology 2000, 17:1237-1243.
    • (2000) International Journal of Oncology , vol.17 , pp. 1237-1243
    • Noti, J.D.1
  • 54
    • 0029884455 scopus 로고    scopus 로고
    • The identification of osteopontin as a metastasis-related gene product in a rodent mammary tumour model
    • Oates A.J., Barraclough R., Rudland P.S. The identification of osteopontin as a metastasis-related gene product in a rodent mammary tumour model. Oncogene 1996, 13:97-104.
    • (1996) Oncogene , vol.13 , pp. 97-104
    • Oates, A.J.1    Barraclough, R.2    Rudland, P.S.3
  • 55
    • 0033595125 scopus 로고    scopus 로고
    • Osteopontin induces increased invasiveness and plasminogen activator expression of human mammary epithelial cells
    • Tuck A.B., Arsenault D.M., O'Malley F.P., et al. Osteopontin induces increased invasiveness and plasminogen activator expression of human mammary epithelial cells. Oncogene 1999, 18:4237-4246.
    • (1999) Oncogene , vol.18 , pp. 4237-4246
    • Tuck, A.B.1    Arsenault, D.M.2    O'Malley, F.P.3
  • 57
    • 0030926461 scopus 로고    scopus 로고
    • Osteopontin and p53 expression are associated with tumor progression in a case of synchronous, bilateral, invasive mammary carcinomas
    • Tuck A.B., O'Malley F.P., Singhal H., et al. Osteopontin and p53 expression are associated with tumor progression in a case of synchronous, bilateral, invasive mammary carcinomas. Archives of Pathology & Laboratory Medicine 1997, 121:578-584.
    • (1997) Archives of Pathology & Laboratory Medicine , vol.121 , pp. 578-584
    • Tuck, A.B.1    O'Malley, F.P.2    Singhal, H.3
  • 60
    • 44649088833 scopus 로고    scopus 로고
    • Systemic endocrine instigation of indolent tumor growth requires osteopontin
    • McAllister S.S., Gifford A.M., Greiner A.L., et al. Systemic endocrine instigation of indolent tumor growth requires osteopontin. Cell 2008, 133:994-1005.
    • (2008) Cell , vol.133 , pp. 994-1005
    • McAllister, S.S.1    Gifford, A.M.2    Greiner, A.L.3
  • 61
    • 80855128100 scopus 로고    scopus 로고
    • Periostin expression and epithelial-mesenchymal transition in cancer: a review and an update
    • Morra L., Moch H. Periostin expression and epithelial-mesenchymal transition in cancer: a review and an update. Virchows Archiv: An International Journal of Pathology 2011, 459:465-475.
    • (2011) Virchows Archiv: An International Journal of Pathology , vol.459 , pp. 465-475
    • Morra, L.1    Moch, H.2
  • 62
    • 77951235064 scopus 로고    scopus 로고
    • Interaction between periostin and BMP-1 promotes proteolytic activation of lysyl oxidase
    • Maruhashi T., Kii I., Saito M., Kudo A. Interaction between periostin and BMP-1 promotes proteolytic activation of lysyl oxidase. Journal of Biological Chemistry 2010, 285:13294-13303.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 13294-13303
    • Maruhashi, T.1    Kii, I.2    Saito, M.3    Kudo, A.4
  • 63
    • 84855425160 scopus 로고    scopus 로고
    • Interactions between cancer stem cells and their niche govern metastatic colonization
    • Malanchi I., Santamaria-Martinez A., Susanto E., et al. Interactions between cancer stem cells and their niche govern metastatic colonization. Nature 2012, 481:85-89.
    • (2012) Nature , vol.481 , pp. 85-89
    • Malanchi, I.1    Santamaria-Martinez, A.2    Susanto, E.3
  • 64
    • 0037318744 scopus 로고    scopus 로고
    • Elevated serum periostin levels in patients with bone metastases from breast but not lung cancer
    • Sasaki H., Yu C.Y., Dai M., et al. Elevated serum periostin levels in patients with bone metastases from breast but not lung cancer. Breast Cancer Research and Treatment 2003, 77:245-252.
    • (2003) Breast Cancer Research and Treatment , vol.77 , pp. 245-252
    • Sasaki, H.1    Yu, C.Y.2    Dai, M.3
  • 65
    • 21244471421 scopus 로고    scopus 로고
    • Stromal remodeling and SPARC (secreted protein acid rich in cysteine) expression in invasive ductal carcinomas of the breast
    • Barth P.J., Moll R., Ramaswamy A. Stromal remodeling and SPARC (secreted protein acid rich in cysteine) expression in invasive ductal carcinomas of the breast. Virchows Archiv: An International Journal of Pathology 2005, 446:532-536.
    • (2005) Virchows Archiv: An International Journal of Pathology , vol.446 , pp. 532-536
    • Barth, P.J.1    Moll, R.2    Ramaswamy, A.3
  • 66
    • 0032401846 scopus 로고    scopus 로고
    • SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines
    • Gilles C., Bassuk J.A., Pulyaeva H., Sage E.H., Foidart J.M., Thompson E.W. SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines. Cancer Research 1998, 58:5529-5536.
    • (1998) Cancer Research , vol.58 , pp. 5529-5536
    • Gilles, C.1    Bassuk, J.A.2    Pulyaeva, H.3    Sage, E.H.4    Foidart, J.M.5    Thompson, E.W.6
  • 67
    • 23144461051 scopus 로고    scopus 로고
    • Genes that mediate breast cancer metastasis to lung
    • Minn A.J., Gupta G.P., Siegel P.M., et al. Genes that mediate breast cancer metastasis to lung. Nature 2005, 436:518-524.
    • (2005) Nature , vol.436 , pp. 518-524
    • Minn, A.J.1    Gupta, G.P.2    Siegel, P.M.3
  • 69
    • 0031418062 scopus 로고    scopus 로고
    • Expression of osteonectin mRNA in human breast tumours is inversely correlated with oestrogen receptor content
    • Graham J.D., Balleine R.L., Milliken J.S., Bilous A.M., Clarke C.L. Expression of osteonectin mRNA in human breast tumours is inversely correlated with oestrogen receptor content. European Journal of Cancer 1997, 33:1654-1660.
    • (1997) European Journal of Cancer , vol.33 , pp. 1654-1660
    • Graham, J.D.1    Balleine, R.L.2    Milliken, J.S.3    Bilous, A.M.4    Clarke, C.L.5
  • 70
    • 77956408178 scopus 로고    scopus 로고
    • Stromal CD10 and SPARC expression in ductal carcinoma in situ (DCIS) patients predicts disease recurrence
    • Witkiewicz A.K., Freydin B., Chervoneva I., et al. Stromal CD10 and SPARC expression in ductal carcinoma in situ (DCIS) patients predicts disease recurrence. Cancer Biology & Therapy 2010, 10:391-396.
    • (2010) Cancer Biology & Therapy , vol.10 , pp. 391-396
    • Witkiewicz, A.K.1    Freydin, B.2    Chervoneva, I.3
  • 71
    • 77953549226 scopus 로고    scopus 로고
    • SPARC (osteonectin) in breast tumors of different histologic types and its role in the outcome of invasive ductal carcinoma
    • Hsiao Y.H., Lien H.C., Hwa H.L., Kuo W.H., Chang K.J., Hsieh F.J. SPARC (osteonectin) in breast tumors of different histologic types and its role in the outcome of invasive ductal carcinoma. Breast Journal 2010, 16:305-308.
    • (2010) Breast Journal , vol.16 , pp. 305-308
    • Hsiao, Y.H.1    Lien, H.C.2    Hwa, H.L.3    Kuo, W.H.4    Chang, K.J.5    Hsieh, F.J.6
  • 74
    • 0030868422 scopus 로고    scopus 로고
    • Thrombospondin-1 and transforming growth factor-beta l promote breast tumor cell invasion through up-regulation of the plasminogen/plasmin system
    • [discussion 99-500]
    • Albo D., Berger D.H., Wang T.N., Hu X., Rothman V., Tuszynski G.P. Thrombospondin-1 and transforming growth factor-beta l promote breast tumor cell invasion through up-regulation of the plasminogen/plasmin system. Surgery 1997, 122:493-499. [discussion 99-500].
    • (1997) Surgery , vol.122 , pp. 493-499
    • Albo, D.1    Berger, D.H.2    Wang, T.N.3    Hu, X.4    Rothman, V.5    Tuszynski, G.P.6
  • 75
    • 79955064062 scopus 로고    scopus 로고
    • SFRP-1 binds via its netrin-related motif to the N-module of thrombospondin-1 and blocks thrombospondin-1 stimulation of MDA-MB-231 breast carcinoma cell adhesion and migration
    • Martin-Manso G., Calzada M.J., Chuman Y., et al. sFRP-1 binds via its netrin-related motif to the N-module of thrombospondin-1 and blocks thrombospondin-1 stimulation of MDA-MB-231 breast carcinoma cell adhesion and migration. Archives of Biochemistry and Biophysics 2011, 509:147-156.
    • (2011) Archives of Biochemistry and Biophysics , vol.509 , pp. 147-156
    • Martin-Manso, G.1    Calzada, M.J.2    Chuman, Y.3
  • 78
    • 84863149986 scopus 로고    scopus 로고
    • Comparative profiling of plasma proteome from breast cancer patients reveals thrombospondin-1 and BRWD3 as serological biomarkers
    • Suh E.J., Kabir M.H., Kang U.B., et al. Comparative profiling of plasma proteome from breast cancer patients reveals thrombospondin-1 and BRWD3 as serological biomarkers. Experimental & Molecular Medicine 2012, 44:36-44.
    • (2012) Experimental & Molecular Medicine , vol.44 , pp. 36-44
    • Suh, E.J.1    Kabir, M.H.2    Kang, U.B.3
  • 79
    • 38449086640 scopus 로고    scopus 로고
    • Angiogenic characteristics of circulating and tumoural thrombospondin-1 in breast cancer
    • Byrne G.J., Hayden K.E., McDowell G., et al. Angiogenic characteristics of circulating and tumoural thrombospondin-1 in breast cancer. International Journal of Oncology 2007, 31:1127-1132.
    • (2007) International Journal of Oncology , vol.31 , pp. 1127-1132
    • Byrne, G.J.1    Hayden, K.E.2    McDowell, G.3
  • 80
    • 0028306856 scopus 로고
    • Plasma thrombospondin levels in patients with gynecologic malignancies
    • Nathan F.E., Hernandez E., Dunton C.J., et al. Plasma thrombospondin levels in patients with gynecologic malignancies. Cancer 1994, 73:2853-2858.
    • (1994) Cancer , vol.73 , pp. 2853-2858
    • Nathan, F.E.1    Hernandez, E.2    Dunton, C.J.3
  • 81
    • 28644432204 scopus 로고    scopus 로고
    • VEGFR1-positive haematopoietic bone marrow progenitors initiate the pre-metastatic niche
    • Kaplan R.N., Riba R.D., Zacharoulis S., et al. VEGFR1-positive haematopoietic bone marrow progenitors initiate the pre-metastatic niche. Nature 2005, 438:820-827.
    • (2005) Nature , vol.438 , pp. 820-827
    • Kaplan, R.N.1    Riba, R.D.2    Zacharoulis, S.3
  • 82
    • 57849100048 scopus 로고    scopus 로고
    • Hypoxia-induced lysyl oxidase is a critical mediator of bone marrow cell recruitment to form the premetastatic niche
    • Erler J.T., Bennewith K.L., Cox T.R., et al. Hypoxia-induced lysyl oxidase is a critical mediator of bone marrow cell recruitment to form the premetastatic niche. Cancer Cell 2009, 15:35-44.
    • (2009) Cancer Cell , vol.15 , pp. 35-44
    • Erler, J.T.1    Bennewith, K.L.2    Cox, T.R.3
  • 83
    • 84857189202 scopus 로고    scopus 로고
    • Extracellular matrix players in metastatic niches
    • Oskarsson T., Massague J. Extracellular matrix players in metastatic niches. EMBO Journal 2012, 31:254-256.
    • (2012) EMBO Journal , vol.31 , pp. 254-256
    • Oskarsson, T.1    Massague, J.2
  • 84
    • 76249097588 scopus 로고    scopus 로고
    • Incorporation of tenascin-C into the extracellular matrix by periostin underlies an extracellular meshwork architecture
    • Kii I., Nishiyama T., Li M., et al. Incorporation of tenascin-C into the extracellular matrix by periostin underlies an extracellular meshwork architecture. Journal of Biological Chemistry 2010, 285:2028-2039.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 2028-2039
    • Kii, I.1    Nishiyama, T.2    Li, M.3
  • 85
    • 38949202980 scopus 로고    scopus 로고
    • Extracellular matrix signature identifies breast cancer subgroups with different clinical outcome
    • Bergamaschi A., Tagliabue E., Sorlie T., et al. Extracellular matrix signature identifies breast cancer subgroups with different clinical outcome. Journal of Pathology 2008, 214:357-367.
    • (2008) Journal of Pathology , vol.214 , pp. 357-367
    • Bergamaschi, A.1    Tagliabue, E.2    Sorlie, T.3
  • 86
    • 58149334773 scopus 로고    scopus 로고
    • Astroma-related gene signature predicts resistance to neoadjuvant chemotherapy in breast cancer
    • Farmer P., Bonnefoi H., Anderle P., et al. Astroma-related gene signature predicts resistance to neoadjuvant chemotherapy in breast cancer. Nature Medicine 2009, 15:68-74.
    • (2009) Nature Medicine , vol.15 , pp. 68-74
    • Farmer, P.1    Bonnefoi, H.2    Anderle, P.3
  • 87
    • 79955886688 scopus 로고    scopus 로고
    • Knockdown of osteopontin chemosensitizes MDA-MB-231 cells to cyclophosphamide by enhancing apoptosis through activating p38 MAPK pathway
    • Pang H., Cai L., Yang Y., Chen X., Sui G., Zhao C. Knockdown of osteopontin chemosensitizes MDA-MB-231 cells to cyclophosphamide by enhancing apoptosis through activating p38 MAPK pathway. Cancer Biotherapy & Radiopharmaceuticals 2011, 26:165-173.
    • (2011) Cancer Biotherapy & Radiopharmaceuticals , vol.26 , pp. 165-173
    • Pang, H.1    Cai, L.2    Yang, Y.3    Chen, X.4    Sui, G.5    Zhao, C.6
  • 88
    • 84862934553 scopus 로고    scopus 로고
    • Down-regulation of osteopontin expression by RNA interference affects cell proliferation and chemotherapy sensitivity of breast cancer MDA-MB-231 cells
    • Yang L., Wei L., Zhao W., et al. Down-regulation of osteopontin expression by RNA interference affects cell proliferation and chemotherapy sensitivity of breast cancer MDA-MB-231 cells. Molecular Medicine Reports 2012, 5:373-376.
    • (2012) Molecular Medicine Reports , vol.5 , pp. 373-376
    • Yang, L.1    Wei, L.2    Zhao, W.3
  • 90
    • 34249303115 scopus 로고    scopus 로고
    • Regulation of breast cancer response to chemotherapy by fibulin-1
    • Pupa S.M., Giuffre S., Castiglioni F., et al. Regulation of breast cancer response to chemotherapy by fibulin-1. Cancer Research 2007, 67:4271-4277.
    • (2007) Cancer Research , vol.67 , pp. 4271-4277
    • Pupa, S.M.1    Giuffre, S.2    Castiglioni, F.3
  • 92
    • 20144385541 scopus 로고    scopus 로고
    • Regulation of MDR1 expression and drug resistance by a positive feedback loop involving hyaluronan, phosphoinositide 3-kinase, and ErbB2
    • Misra S., Ghatak S., Toole B.P. Regulation of MDR1 expression and drug resistance by a positive feedback loop involving hyaluronan, phosphoinositide 3-kinase, and ErbB2. Journal of Biological Chemistry 2005, 280:20310-20315.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 20310-20315
    • Misra, S.1    Ghatak, S.2    Toole, B.P.3
  • 93
    • 82955189189 scopus 로고    scopus 로고
    • Macrophages and cathepsin proteases blunt chemotherapeutic response in breast cancer
    • Shree T., Olson O.C., Elie B.T., et al. Macrophages and cathepsin proteases blunt chemotherapeutic response in breast cancer. Genes & Development 2011, 25:2465-2479.
    • (2011) Genes & Development , vol.25 , pp. 2465-2479
    • Shree, T.1    Olson, O.C.2    Elie, B.T.3
  • 94
    • 77950257304 scopus 로고    scopus 로고
    • Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists
    • Yang X.H., Flores L.M., Li Q., et al. Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists. Cancer Research 2010, 70:2256-2263.
    • (2010) Cancer Research , vol.70 , pp. 2256-2263
    • Yang, X.H.1    Flores, L.M.2    Li, Q.3
  • 95
    • 0242659395 scopus 로고    scopus 로고
    • Fibronectin and laminin increase resistance to ionizing radiation and the cytotoxic drug Ukrain in human tumour and normal cells invitro
    • Cordes N., Blaese M.A., Plasswilm L., Rodemann H.P., Van Beuningen D. Fibronectin and laminin increase resistance to ionizing radiation and the cytotoxic drug Ukrain in human tumour and normal cells invitro. International Journal of Radiation Biology 2003, 79:709-720.
    • (2003) International Journal of Radiation Biology , vol.79 , pp. 709-720
    • Cordes, N.1    Blaese, M.A.2    Plasswilm, L.3    Rodemann, H.P.4    Van Beuningen, D.5
  • 96
    • 19944426910 scopus 로고    scopus 로고
    • Osteoprotegerin and osteopontin serum values in postmenopausal advanced breast cancer patients treated with anastrozole
    • Martinetti A., Bajetta E., Ferrari L., et al. Osteoprotegerin and osteopontin serum values in postmenopausal advanced breast cancer patients treated with anastrozole. Endocrine-related Cancer 2004, 11:771-779.
    • (2004) Endocrine-related Cancer , vol.11 , pp. 771-779
    • Martinetti, A.1    Bajetta, E.2    Ferrari, L.3
  • 97
    • 69949101473 scopus 로고    scopus 로고
    • Antioxidant and oncogene rescue of metabolic defects caused by loss of matrix attachment
    • Schafer Z.T., Grassian A.R., Song L., et al. Antioxidant and oncogene rescue of metabolic defects caused by loss of matrix attachment. Nature 2009, 461:109-113.
    • (2009) Nature , vol.461 , pp. 109-113
    • Schafer, Z.T.1    Grassian, A.R.2    Song, L.3
  • 98
    • 84863625224 scopus 로고    scopus 로고
    • ACXCL1 paracrine network links cancer chemoresistance and metastasis
    • Acharyya S., Oskarsson T., Vanharanta S., et al. ACXCL1 paracrine network links cancer chemoresistance and metastasis. Cell 2012, 150:165-178.
    • (2012) Cell , vol.150 , pp. 165-178
    • Acharyya, S.1    Oskarsson, T.2    Vanharanta, S.3
  • 99
    • 77958501473 scopus 로고    scopus 로고
    • DNA damage-mediated induction of a chemoresistant niche
    • Gilbert L.A., Hemann M.T. DNA damage-mediated induction of a chemoresistant niche. Cell 2010, 143:355-366.
    • (2010) Cell , vol.143 , pp. 355-366
    • Gilbert, L.A.1    Hemann, M.T.2
  • 100
    • 79958099193 scopus 로고    scopus 로고
    • Role of periostin in cancer progression and metastasis: inhibition of breast cancer progression and metastasis by anti-periostin antibody in a murine model
    • Kyutoku M., Taniyama Y., Katsuragi N., et al. Role of periostin in cancer progression and metastasis: inhibition of breast cancer progression and metastasis by anti-periostin antibody in a murine model. International Journal of Molecular Medicine 2011, 28:181-186.
    • (2011) International Journal of Molecular Medicine , vol.28 , pp. 181-186
    • Kyutoku, M.1    Taniyama, Y.2    Katsuragi, N.3
  • 101
    • 83655167411 scopus 로고    scopus 로고
    • Inhibition of hyaluronan synthesis in breast cancer cells by 4-methylumbelliferone suppresses tumorigenicity invitro and metastatic lesions of bone invivo
    • Urakawa H., Nishida Y., Wasa J., et al. Inhibition of hyaluronan synthesis in breast cancer cells by 4-methylumbelliferone suppresses tumorigenicity invitro and metastatic lesions of bone invivo. International Journal of Cancer. Journal International du Cancer 2012, 130:454-466.
    • (2012) International Journal of Cancer. Journal International du Cancer , vol.130 , pp. 454-466
    • Urakawa, H.1    Nishida, Y.2    Wasa, J.3
  • 102
    • 79952278967 scopus 로고    scopus 로고
    • The cathepsin K inhibitor odanacatib suppresses bone resorption in women with breast cancer and established bone metastases: results of a 4-week, double-blind, randomized, controlled trial
    • Jensen A.B., Wynne C., Ramirez G., et al. The cathepsin K inhibitor odanacatib suppresses bone resorption in women with breast cancer and established bone metastases: results of a 4-week, double-blind, randomized, controlled trial. Clinical Breast Cancer 2010, 10:452-458.
    • (2010) Clinical Breast Cancer , vol.10 , pp. 452-458
    • Jensen, A.B.1    Wynne, C.2    Ramirez, G.3
  • 103


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